| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Arleth, Lise
University of Copenhagen
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (15/15 displayed)
- 2023Modeling of flexible membrane-bound biomolecular complexes for solution small-angle scatteringcitations
- 2023Aggregative adherence fimbriae form compact structures as seen by SAXScitations
- 2022Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulationcitations
- 2022Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulationcitations
- 2021Mg2+-dependent conformational equilibria in CorA: an integrated view on transport regulation
- 2021The microscopic distribution of hydrophilic polymers in interpenetrating polymer networks (IPNs) of medical grade siliconecitations
- 2020Assessment of structure factors for analysis of small-angle scattering data from desired or undesired aggregatescitations
- 2020Dispersion state of TiO2 pigment particles studied by ultra-small-angle X-ray scattering revealing dependence on dispersant but limited change during drying of paint coatingcitations
- 2019Circularized and solubility-enhanced MSPs facilitate simple and high-yield production of stable nanodiscs for studies of membrane proteins in solutioncitations
- 2016Construction of insulin 18-mer nanoassemblies driven by coordination to Iron(II) and Zinc(II) ions at distinct sitescitations
- 2016Dimeric peptides with three different linkers self-assemble with phospholipids to form peptide nanodiscs that stabilize membrane proteinscitations
- 2015Small-angle scattering determination of the shape and localization of human cytochrome P450 embedded in a phospholipid nanodisc environmentcitations
- 2014Stealth carriers for low-resolution structure determination of membrane proteins in solutioncitations
- 2013Self-assembly of designed coiled coil peptides studied by small-angle X-ray scattering and analytical ultracentrifugationcitations
- 2013WillItFitcitations
Places of action
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article
Self-assembly of designed coiled coil peptides studied by small-angle X-ray scattering and analytical ultracentrifugation
Abstract
α-Helical coiled coil structures, which are noncovalently associated heptad repeat peptide sequences, are ubiquitous in nature. Similar amphipathic repeat sequences have also been found in helix-containing proteins and have played a central role in de novo design of proteins. In addition, they are promising tools for the construction of nanomaterials. Small-angle X-ray scattering (SAXS) has emerged as a new biophysical technique for elucidation of protein topology. Here, we describe a systematic study of the self-assembly of a small ensemble of coiled coil sequences using SAXS and analytical ultracentrifugation (AUC), which was correlated with molecular dynamics simulations. Our results show that even minor sequence changes have an effect on the folding topology and the self-assembly and that these differences can be observed by a combination of AUC, SAXS, and circular dichroism spectroscopy. A small difference in these methods was observed, as SAXS for one peptide and revealed the presence of a population of longer aggregates, which was not observed by AUC.